Early‐Stage Folding in Proteins (In Silico) Sequence‐to‐Structure Relation | Zendy

Michał Bryliński | Zendy; Leszek Konieczny | Zendy; Patryk Czerwonko | Zendy; Wiktor Jurkowski | Zendy; Irena Roterman | Zendy

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Early‐Stage Folding in Proteins (In Silico) Sequence‐to‐Structure Relation

Author(s) -

Michał Bryliński,

Leszek Konieczny,

Patryk Czerwonko,

Wiktor Jurkowski,

Irena Roterman

Publication year - 2005

Publication title -

biomed research international

Language(s) - English

Resource type - Journals

eISSN - 2314-6141

pISSN - 2314-6133

DOI - 10.1155/jbb.2005.65

Subject(s) - sequence (biology) , loop modeling , folding (dsp implementation) , protein data bank (rcsb pdb) , tetrapeptide , protein folding , structural alignment , structural motif , protein structure , computational biology , mathematics , computer science , protein structure prediction , sequence alignment , peptide sequence , biology , stereochemistry , genetics , chemistry , peptide , biochemistry , gene , electrical engineering , engineering

A sequence-to-structure library has been created based on the complete PDB database. The tetrapeptide was selected as a unit representing a well-defined structural motif. Seven structural forms were introduced for structure classification. The early-stage folding conformations were used as the objects for structure analysis and classification. The degree of determinability was estimated for the sequence-to-structure and structure-to-sequence relations. Probability calculus and informational entropy were applied for quantitative estimation of the mutual relation between them. The structural motifs representing different forms of loops and bends were found to favor particular sequences in structure-to-sequence analysis.

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